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New page: left|200px<br /><applet load="1d8z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d8z" /> '''SOLUTION STRUCTURE OF THE FIRST RNA-BINDING ...
 
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[[Image:1d8z.gif|left|200px]]<br /><applet load="1d8z" size="450" color="white" frame="true" align="right" spinBox="true"
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'''SOLUTION STRUCTURE OF THE FIRST RNA-BINDING DOMAIN (RBD1) OF HU ANTIGEN C (HUC)'''<br />


==Overview==
==SOLUTION STRUCTURE OF THE FIRST RNA-BINDING DOMAIN (RBD1) OF HU ANTIGEN C (HUC)==
Hu antigen C (HuC) has three RNA-binding domains (RBDs). The N-terminal, two, RBD1 and RBD2, are linked in tandem and bind to the AU-rich elements, (AREs) in the 3'-untranslated region of particular mRNAs. The solution, structures of HuC RBD1 and RBD2 were determined by NMR methods. The HuC, RBD1 and RBD2 structures are quite similar to those of Sxl RBD1 and RBD2, respectively. The individual RBDs of HuC, RBD1 and RBD2 in isolation can, interact rather weakly with the minimal ARE motif, AUUUA, while the, didomain fragment, RBD1-RBD2, of HuC binds more tightly to a longer ARE, RNA, UAUUUAUUUU. Chemical shift perturbations by the longer RNA on HuC, RBD1-RBD2 were mapped on and around the two beta-sheets and on the, C-terminal region of RBD1. The HuC RBD1-RBD2 residues that exhibited, significant chemical shift perturbations coincide with those conserved in, Sxl RBD1-RBD2. These data indicate that the RNA-binding characteristics of, the HuC and Sxl didomain fragments are similar, even though the target, RNAs and the biological functions of the proteins are different.
<StructureSection load='1d8z' size='340' side='right'caption='[[1d8z]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d8z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D8Z FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d8z OCA], [https://pdbe.org/1d8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d8z RCSB], [https://www.ebi.ac.uk/pdbsum/1d8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d8z ProSAT], [https://www.topsan.org/Proteins/RSGI/1d8z TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ELAV3_MOUSE ELAV3_MOUSE] Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF mRNA. May also bind poly-A tracts via RRM 3. May be involved in neuronal differentiation and maintenance.<ref>PMID:9016658</ref> <ref>PMID:10734193</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d8/1d8z_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1d8z ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hu antigen C (HuC) has three RNA-binding domains (RBDs). The N-terminal two, RBD1 and RBD2, are linked in tandem and bind to the AU-rich elements (AREs) in the 3'-untranslated region of particular mRNAs. The solution structures of HuC RBD1 and RBD2 were determined by NMR methods. The HuC RBD1 and RBD2 structures are quite similar to those of Sxl RBD1 and RBD2, respectively. The individual RBDs of HuC, RBD1 and RBD2 in isolation can interact rather weakly with the minimal ARE motif, AUUUA, while the didomain fragment, RBD1-RBD2, of HuC binds more tightly to a longer ARE RNA, UAUUUAUUUU. Chemical shift perturbations by the longer RNA on HuC RBD1-RBD2 were mapped on and around the two beta-sheets and on the C-terminal region of RBD1. The HuC RBD1-RBD2 residues that exhibited significant chemical shift perturbations coincide with those conserved in Sxl RBD1-RBD2. These data indicate that the RNA-binding characteristics of the HuC and Sxl didomain fragments are similar, even though the target RNAs and the biological functions of the proteins are different.


==About this Structure==
NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C.,Inoue M, Muto Y, Sakamoto H, Yokoyama S Nucleic Acids Res. 2000 Apr 15;28(8):1743-50. PMID:10734193<ref>PMID:10734193</ref>
1D8Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D8Z OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C., Inoue M, Muto Y, Sakamoto H, Yokoyama S, Nucleic Acids Res. 2000 Apr 15;28(8):1743-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10734193 10734193]
</div>
<div class="pdbe-citations 1d8z" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Inoue M]]
[[Category: Inoue, M.]]
[[Category: Muto Y]]
[[Category: Muto, Y.]]
[[Category: Sakamoto H]]
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[[Category: Yokoyama S]]
[[Category: Sakamoto, H.]]
[[Category: Yokoyama, S.]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rna-binding domain]]
[[Category: rsgi]]
[[Category: structural genomics]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:05:33 2007''

Latest revision as of 11:23, 22 May 2024

SOLUTION STRUCTURE OF THE FIRST RNA-BINDING DOMAIN (RBD1) OF HU ANTIGEN C (HUC)SOLUTION STRUCTURE OF THE FIRST RNA-BINDING DOMAIN (RBD1) OF HU ANTIGEN C (HUC)

Structural highlights

1d8z is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

ELAV3_MOUSE Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF mRNA. May also bind poly-A tracts via RRM 3. May be involved in neuronal differentiation and maintenance.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Hu antigen C (HuC) has three RNA-binding domains (RBDs). The N-terminal two, RBD1 and RBD2, are linked in tandem and bind to the AU-rich elements (AREs) in the 3'-untranslated region of particular mRNAs. The solution structures of HuC RBD1 and RBD2 were determined by NMR methods. The HuC RBD1 and RBD2 structures are quite similar to those of Sxl RBD1 and RBD2, respectively. The individual RBDs of HuC, RBD1 and RBD2 in isolation can interact rather weakly with the minimal ARE motif, AUUUA, while the didomain fragment, RBD1-RBD2, of HuC binds more tightly to a longer ARE RNA, UAUUUAUUUU. Chemical shift perturbations by the longer RNA on HuC RBD1-RBD2 were mapped on and around the two beta-sheets and on the C-terminal region of RBD1. The HuC RBD1-RBD2 residues that exhibited significant chemical shift perturbations coincide with those conserved in Sxl RBD1-RBD2. These data indicate that the RNA-binding characteristics of the HuC and Sxl didomain fragments are similar, even though the target RNAs and the biological functions of the proteins are different.

NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C.,Inoue M, Muto Y, Sakamoto H, Yokoyama S Nucleic Acids Res. 2000 Apr 15;28(8):1743-50. PMID:10734193[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Abe R, Sakashita E, Yamamoto K, Sakamoto H. Two different RNA binding activities for the AU-rich element and the poly(A) sequence of the mouse neuronal protein mHuC. Nucleic Acids Res. 1996 Dec 15;24(24):4895-901. PMID:9016658
  2. ↑ Inoue M, Muto Y, Sakamoto H, Yokoyama S. NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C. Nucleic Acids Res. 2000 Apr 15;28(8):1743-50. PMID:10734193
  3. ↑ Inoue M, Muto Y, Sakamoto H, Yokoyama S. NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C. Nucleic Acids Res. 2000 Apr 15;28(8):1743-50. PMID:10734193
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